VAPB_SALTY
ID VAPB_SALTY Reviewed; 75 AA.
AC Q7CPV2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Antitoxin VapB;
GN Name=vapB; OrderedLocusNames=STM3034;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION AS AN ANTITOXIN, AND INDUCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=19400780; DOI=10.1111/j.1365-2958.2009.06694.x;
RA Winther K.S., Gerdes K.;
RT "Ectopic production of VapCs from Enterobacteria inhibits translation and
RT trans-activates YoeB mRNA interferase.";
RL Mol. Microbiol. 72:918-930(2009).
RN [3]
RP FUNCTION AS AN ANTITOXIN.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=21502523; DOI=10.1073/pnas.1019587108;
RA Winther K.S., Gerdes K.;
RT "Enteric virulence associated protein VapC inhibits translation by cleavage
RT of initiator tRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7403-7407(2011).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in E.coli neutralizes the effect of cognate toxin VapC.
CC {ECO:0000269|PubMed:19400780, ECO:0000269|PubMed:21502523}.
CC -!- SUBUNIT: Forms a complex with toxin VapC. {ECO:0000305}.
CC -!- INDUCTION: Induced by amino acid starvation and by chloramphenicol
CC treatment. {ECO:0000269|PubMed:19400780}.
CC -!- SIMILARITY: Belongs to the VapB family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21910.1; -; Genomic_DNA.
DR RefSeq; NP_461951.1; NC_003197.2.
DR RefSeq; WP_000557549.1; NC_003197.2.
DR PDB; 6IFM; X-ray; 2.80 A; B/D/F/H=1-68.
DR PDBsum; 6IFM; -.
DR AlphaFoldDB; Q7CPV2; -.
DR SMR; Q7CPV2; -.
DR STRING; 99287.STM3034; -.
DR PaxDb; Q7CPV2; -.
DR EnsemblBacteria; AAL21910; AAL21910; STM3034.
DR GeneID; 1254557; -.
DR KEGG; stm:STM3034; -.
DR PATRIC; fig|99287.12.peg.3212; -.
DR HOGENOM; CLU_162018_3_2_6; -.
DR OMA; VFTNNRS; -.
DR PhylomeDB; Q7CPV2; -.
DR BioCyc; SENT99287:STM3034-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR007159; SpoVT-AbrB_dom.
DR InterPro; IPR037914; SpoVT-AbrB_sf.
DR SUPFAM; SSF89447; SSF89447; 1.
DR PROSITE; PS51740; SPOVT_ABRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..75
FT /note="Antitoxin VapB"
FT /id="PRO_0000410982"
FT DOMAIN 3..45
FT /note="SpoVT-AbrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6IFM"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6IFM"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6IFM"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6IFM"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6IFM"
SQ SEQUENCE 75 AA; 8515 MW; 0A33AC546A04F78D CRC64;
MHTTLFFSNR TQAVRLPKSI SFPEDVKHVE IIAVGRSRII TPVGESWDSW FDGEGASTDF
MSTREQPAVQ EREGF
